English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Spatial distribution and activity of Na +/K +-ATPase in lipid bilayer membranes with phase boundaries

Bhatia, T., Cornelius, F., Brewer, J., Bagatolli, L. A., Simonsen, A. C., Ipsen, J. H., et al. (2016). Spatial distribution and activity of Na +/K +-ATPase in lipid bilayer membranes with phase boundaries. Biochimica et Biophysica Acta (BBA) - Biomembranes, 1858(6), 1390-1399. doi:10.1016/j.bbamem.2016.03.015.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-22B4-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-BD0D-8
Genre: Journal Article

Files

show Files
hide Files
:
2260642.pdf (Publisher version), 4MB
 
File Permalink:
-
Name:
2260642.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute of Colloids and Interfaces, MTKG; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
Manuskript.pdf (Any fulltext), 10MB
 
File Permalink:
-
Name:
Manuskript.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute of Colloids and Interfaces, MTKG; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Bhatia, Tripta1, Author              
Cornelius, Flemming, Author
Brewer, Jonathan, Author
Bagatolli, Luis A., Author
Simonsen, Adam C., Author
Ipsen, John H., Author
Mouritsen, Ole G., Author
Affiliations:
1Rumiana Dimova, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863328              

Content

show
hide
Free keywords: Membranes; Na +/K +-ATPase; Giant Unilamellar Vesicles; Domains; Membrane Protein; Protein-Lipid Interaction; Membrane Biophysics
 Abstract: Abstract We have reconstituted functional Na +/K +-ATPase (NKA) into giant unilamellar vesicles (GUVs) of well-defined binary and ternary lipid composition including cholesterol. The activity of the membrane system can be turned on and off by ATP. The hydrolytic activity of \NKA\} is found to depend on membrane phase, and the water relaxation in the membrane on the presence of NKA. By collapsing and fixating the \{GUVs\} onto a solid support and using high-resolution atomic-force microscopy (AFM) imaging we determine the protein orientation and spatial distribution at the single-molecule level and find that \{NKA\} is preferentially located at l o/l d interfaces in two-phase \{GUVs\ and homogeneously distributed in single-phase GUVs. When turned active, the membrane is found to unbind from the support suggesting that the protein function leads to a softening of the membrane.

Details

show
hide
Language(s):
 Dates: 2016-03-162016
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: DOI: 10.1016/j.bbamem.2016.03.015
BibTex Citekey: Bhatia2016
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Biochimica et Biophysica Acta (BBA) - Biomembranes
  Abbreviation : BBA
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 1858 (6) Sequence Number: - Start / End Page: 1390 - 1399 Identifier: ISSN: 0005-2736